3rjo
From Proteopedia
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==Crystal Structure of ERAP1 Peptide Binding Domain== | ==Crystal Structure of ERAP1 Peptide Binding Domain== | ||
| - | <StructureSection load='3rjo' size='340' side='right' caption='[[3rjo]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='3rjo' size='340' side='right'caption='[[3rjo]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3rjo]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3rjo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RJO FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rjo OCA], [https://pdbe.org/3rjo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rjo RCSB], [https://www.ebi.ac.uk/pdbsum/3rjo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rjo ProSAT]</span></td></tr> |
</table> | </table> | ||
| - | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ERAP1_HUMAN ERAP1_HUMAN]] Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney.<ref>PMID:15908954</ref> <ref>PMID:16286653</ref> <ref>PMID:21478864</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 3rjo" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Aminopeptidase|Aminopeptidase]] | + | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Gandhi | + | [[Category: Large Structures]] |
| - | [[Category: Guo | + | [[Category: Gandhi A]] |
| - | [[Category: Lakshminarasimhan | + | [[Category: Guo H-C]] |
| - | + | [[Category: Lakshminarasimhan D]] | |
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Current revision
Crystal Structure of ERAP1 Peptide Binding Domain
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